Structure of PDB 6wr0 Chain C Binding Site BS02

Receptor Information
>6wr0 Chain C (length=474) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHH
QLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAM
ATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVI
SLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTL
EKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAG
PDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLY
EEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDS
SIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPS
VSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGI
PKVVFLIDSFKVKIKVRQAWREAQ
Ligand information
Ligand IDU7P
InChIInChI=1S/C24H29NO/c1-23-11-9-18(26)14-17(23)5-6-19-21-8-7-20(16-4-3-13-25-15-16)24(21,2)12-10-22(19)23/h3-4,7,13-15,19,21-22H,5-6,8-12H2,1-2H3/t19-,21-,22-,23-,24+/m0/s1
InChIKeyGYJZZAJJENTSTP-NHFPKVKZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7C[C@]12CCC(=O)C=C1CC[C@@H]3[C@@H]2CC[C@]4([C@H]3CC=C4c5cccnc5)C
CACTVS 3.385C[C]12CCC(=O)C=C1CC[CH]3[CH]2CC[C]4(C)[CH]3CC=C4c5cccnc5
ACDLabs 12.01C35C2C(C)(C(c1cnccc1)=CC2)CCC3C4(C(=CC(=O)CC4)CC5)C
OpenEye OEToolkits 2.0.7CC12CCC(=O)C=C1CCC3C2CCC4(C3CC=C4c5cccnc5)C
CACTVS 3.385C[C@]12CCC(=O)C=C1CC[C@@H]3[C@@H]2CC[C@@]4(C)[C@H]3CC=C4c5cccnc5
FormulaC24 H29 N O
Name(8alpha)-17-(pyridin-3-yl)androsta-4,16-dien-3-one;
3-keto-delta4-abiraterone analog
ChEMBLCHEMBL132778
DrugBank
ZINCZINC000003932545
PDB chain6wr0 Chain C Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6wr0 Human cytochrome P450 17A1 structures with metabolites of prostate cancer drug abiraterone reveal substrate-binding plasticity and a second binding site.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		A113 N202 D298 A302 T306 V482
Binding residue
(residue number reindexed from 1)		A84 N173 D269 A273 T277 V453
Annotation score2
Binding affinityBindingDB: IC50=6.1nM
Enzymatic activity
Catalytic site (original residue number in PDB) T306 F435 C442
Catalytic site (residue number reindexed from 1) T277 F406 C413
Enzyme Commision number 1.14.14.19: steroid 17alpha-monooxygenase.
1.14.14.32: 17alpha-hydroxyprogesterone deacetylase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0004508 steroid 17-alpha-monooxygenase activity
GO:0005506 iron ion binding
GO:0008395 steroid hydroxylase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016829 lyase activity
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006694 steroid biosynthetic process
GO:0006702 androgen biosynthetic process
GO:0006704 glucocorticoid biosynthetic process
GO:0007548 sex differentiation
GO:0008202 steroid metabolic process
GO:0042445 hormone metabolic process
GO:0042446 hormone biosynthetic process
GO:0042448 progesterone metabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0030424 axon
GO:0043025 neuronal cell body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6wr0, PDBe:6wr0, PDBj:6wr0
PDBsum6wr0
PubMed36773804
UniProtP05093|CP17A_HUMAN Steroid 17-alpha-hydroxylase/17,20 lyase (Gene Name=CYP17A1)

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